X-RAY STRUCTURES OF ISOFORMS OF THE ACTIN-BINDING PROTEIN PROFILIN THAT DIFFER IN THEIR AFFINITY FOR PHOSPHATIDYLINOSITOL PHOSPHATES
X-RAY STRUCTURES OF ISOFORMS OF THE ACTIN-BINDING PROTEIN PROFILIN THAT DIFFER IN THEIR AFFINITY FOR PHOSPHATIDYLINOSITOL PHOSPHATES
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DOI：
10.1073/pnas.91.18.8636
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发表时间：
1994-08-30
影响因子：
11.1
通讯作者：
ALMO, SC
中科院分区：
文献类型：
--
作者：
FEDOROV, AA;MAGNUS, KA;ALMO, SC
我们确定了阿米巴profilin I和profilin II的结构，通过X-射线晶体学在2.0和2.8埃的分辨率，分别。变形虫profilins的多肽折叠和肌动蛋白结合表面与牛和人profilins非常相似。两种阿米巴同种型的静电势表面不同。两个领域的高正电位的表面上的profilin II的候选人结合位点的磷脂酰肌醇磷酸。这些位点与肌动蛋白结合位点的接近为肌动蛋白和脂质之间竞争结合profilin提供了解释。
We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 Angstrom, respectively. The polypeptide folds and the actin-binding surfaces of the amoeba profilins are very similar to those of bovine and human profilins. The electrostatic potential surfaces of the two Acanthamoeba isoforms differ. Two areas of high positive potential on the surface of profilin II are candidate binding sites for phosphatidylinositol phosphates. The proximity of these sites to the actin binding site provides an explanation for the competition between actin and lipids for binding profilin.